Suicide recombination substrates yield covalent lambda integrase-DNA complexes and lead to identification of the active site tyrosine.

@article{Pargellis1988SuicideRS,
  title={Suicide recombination substrates yield covalent lambda integrase-DNA complexes and lead to identification of the active site tyrosine.},
  author={Chris Pargellis and Simone E. Nunes-D{\"u}by and L M de Vargas and Arthur Landy},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 16},
  pages={
          7678-85
        }
}
High levels of covalent integrase-DNA complexes accumulate when suicide substrates containing a medial nick within the overlap region are nicked by lambda integrase protein. The tyrosine residue at position 342 is shown to form a covalent bond with DNA at the sites of strand exchange. A mutant integrase in which this tyrosine is changed to phenylalanine is devoid of both topoisomerase and recombinase activity but still binds to both core- and arm-type DNA binding sites with an affinity… CONTINUE READING

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